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aleuria aurantia lectin aal  (Vector Laboratories)
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Vector Laboratories aleuria aurantia lectin aal
Evidence that anti-Gal IgG molecules have altered glycosylation in patients with cirrhosis. Briefly, either HSA (column 1) or synthetic alpha-Gal-linked HSA (columns 2 and 3) was plated onto 96-well plates and incubated with human sera from four healthy control individuals or from three individuals with cirrhosis. The captured IgG was detected by using either anti-human IgG-conjugated secondary antibody (columns 1 and 2) or the fucose-specific <t>lectin</t> <t>AAL</t> (column 3).
Aleuria Aurantia Lectin Aal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Evidence that anti-Gal IgG molecules have altered glycosylation in patients with cirrhosis. Briefly, either HSA (column 1) or synthetic alpha-Gal-linked HSA (columns 2 and 3) was plated onto 96-well plates and incubated with human sera from four healthy control individuals or from three individuals with cirrhosis. The captured IgG was detected by using either anti-human IgG-conjugated secondary antibody (columns 1 and 2) or the fucose-specific lectin AAL (column 3).

Journal:

Article Title: Increased Levels of Galactose-Deficient Anti-Gal Immunoglobulin G in the Sera of Hepatitis C Virus-Infected Individuals with Fibrosis and Cirrhosis ▿

doi: 10.1128/JVI.01600-07

Figure Lengend Snippet: Evidence that anti-Gal IgG molecules have altered glycosylation in patients with cirrhosis. Briefly, either HSA (column 1) or synthetic alpha-Gal-linked HSA (columns 2 and 3) was plated onto 96-well plates and incubated with human sera from four healthy control individuals or from three individuals with cirrhosis. The captured IgG was detected by using either anti-human IgG-conjugated secondary antibody (columns 1 and 2) or the fucose-specific lectin AAL (column 3).

Article Snippet: Briefly, lectin extraction was performed using agarose-bound Aleuria aurantia lectin (AAL) (Vector Laboratories, Ventura, CA) and Affi Sep-AAL absorption buffer and elution buffers (GALAB, Germany).

Techniques: Incubation

Evidence that only anti-Gal IgG is reactive with fucose binding lectins. Removal of heterophilic alpha-Gal antibodies prevents lectin reactivity of IgGs from cirrhotic patients. IgGs from either healthy individuals or individuals with cirrhosis were captured from sera by using a mouse anti-human IgG antibody. The amount of captured IgG (lane 1) or the level of AAL lectin reactivity (lane 2) was determined as for Fig. ​Fig.3.3. Samples were precleared either with HSA (lanes 1 and 2) or with alpha-Gal-HSA (lanes 3 and 4) before analysis. H, precleared with HSA; A, precleared with alpha-Gal-HSA.

Journal:

Article Title: Increased Levels of Galactose-Deficient Anti-Gal Immunoglobulin G in the Sera of Hepatitis C Virus-Infected Individuals with Fibrosis and Cirrhosis ▿

doi: 10.1128/JVI.01600-07

Figure Lengend Snippet: Evidence that only anti-Gal IgG is reactive with fucose binding lectins. Removal of heterophilic alpha-Gal antibodies prevents lectin reactivity of IgGs from cirrhotic patients. IgGs from either healthy individuals or individuals with cirrhosis were captured from sera by using a mouse anti-human IgG antibody. The amount of captured IgG (lane 1) or the level of AAL lectin reactivity (lane 2) was determined as for Fig. ​Fig.3.3. Samples were precleared either with HSA (lanes 1 and 2) or with alpha-Gal-HSA (lanes 3 and 4) before analysis. H, precleared with HSA; A, precleared with alpha-Gal-HSA.

Article Snippet: Briefly, lectin extraction was performed using agarose-bound Aleuria aurantia lectin (AAL) (Vector Laboratories, Ventura, CA) and Affi Sep-AAL absorption buffer and elution buffers (GALAB, Germany).

Techniques: Binding Assay

The reactivity of human IgG to the fucose binding lectin AAL is dependent on the type of N-linked glycan attached. (A) IgG from healthy individuals (purchased from Sigma Chemicals) was digested overnight with sialidase (A. ureafaciens) and beta(1-4)-galactosidase (jack bean) to create IgG molecules with the degalactosylated glycans observed in patients with cirrhosis. As a control, a mock sample, treated identically but without enzyme, was used. While IgG purified from healthy individuals had low reactivity with the fucose binding lectin, IgG purified either from cirrhotic individuals or from healthy serum that has been treated with the sialidase and beta-galactosidase had much greater reactivity, indicating that the lectin reactivity is directly associated with the FcA2G0 glycan structure. (B) Glycan analysis of IgG from either mock-treated samples (top) or enzyme-treated samples (bottom) to confirm enzymatic digestion. The major peaks are indicated. For the abbreviations, see the legend to Fig. 5B and C. Additional structures not presented in Fig. ​Fig.5:5: A2G2S1, monosialylated biantennary glycan; FCA2G2S1, monosialylated core fucosylated biantennary N-glycan; FCA2BG2S1, monosialylated core fucosylated biantennary glycan with a bisecting GlcNac; A2G2S2, disialylated biantennary glycan; FCA2BG2S2, disialylated core fucosylated biantennary glycan; FcA2BG2S2, disialylated core fucosylated biantennary glycan with a bisecting GlcNac. (C) Quantification of results shown in panel B. The x axis is the glycan structure as detailed in panel B; the y axis is the relative contribution of each glycan structure to the total N-linked glycan profile. Structures are as in panel B.

Journal:

Article Title: Increased Levels of Galactose-Deficient Anti-Gal Immunoglobulin G in the Sera of Hepatitis C Virus-Infected Individuals with Fibrosis and Cirrhosis ▿

doi: 10.1128/JVI.01600-07

Figure Lengend Snippet: The reactivity of human IgG to the fucose binding lectin AAL is dependent on the type of N-linked glycan attached. (A) IgG from healthy individuals (purchased from Sigma Chemicals) was digested overnight with sialidase (A. ureafaciens) and beta(1-4)-galactosidase (jack bean) to create IgG molecules with the degalactosylated glycans observed in patients with cirrhosis. As a control, a mock sample, treated identically but without enzyme, was used. While IgG purified from healthy individuals had low reactivity with the fucose binding lectin, IgG purified either from cirrhotic individuals or from healthy serum that has been treated with the sialidase and beta-galactosidase had much greater reactivity, indicating that the lectin reactivity is directly associated with the FcA2G0 glycan structure. (B) Glycan analysis of IgG from either mock-treated samples (top) or enzyme-treated samples (bottom) to confirm enzymatic digestion. The major peaks are indicated. For the abbreviations, see the legend to Fig. 5B and C. Additional structures not presented in Fig. ​Fig.5:5: A2G2S1, monosialylated biantennary glycan; FCA2G2S1, monosialylated core fucosylated biantennary N-glycan; FCA2BG2S1, monosialylated core fucosylated biantennary glycan with a bisecting GlcNac; A2G2S2, disialylated biantennary glycan; FCA2BG2S2, disialylated core fucosylated biantennary glycan; FcA2BG2S2, disialylated core fucosylated biantennary glycan with a bisecting GlcNac. (C) Quantification of results shown in panel B. The x axis is the glycan structure as detailed in panel B; the y axis is the relative contribution of each glycan structure to the total N-linked glycan profile. Structures are as in panel B.

Article Snippet: Briefly, lectin extraction was performed using agarose-bound Aleuria aurantia lectin (AAL) (Vector Laboratories, Ventura, CA) and Affi Sep-AAL absorption buffer and elution buffers (GALAB, Germany).

Techniques: Binding Assay, Purification